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cDNA of an arylphorin‐type storage protein from Pieris rapae with parasitism inducible expression by the endoparasitoid wasp Pteromalus puparum
Author(s) -
Zhu JiaYing,
Ye GongYin,
Fang Qi,
Hu Cui,
Akhtar Zunnuraen
Publication year - 2009
Publication title -
insect science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 45
eISSN - 1744-7917
pISSN - 1672-9609
DOI - 10.1111/j.1744-7917.2009.01252.x
Subject(s) - biology , complementary dna , open reading frame , pieris rapae , amino acid , subfamily , rapid amplification of cdna ends , microbiology and biotechnology , peptide sequence , molecular cloning , gene , genetics , botany , lepidoptera genitalia
This report presents the cDNA cloning of a storage protein, PraAry, from Pieris rapae and investigates its expression regulated by parasitism of an endoparasitoid wasp Pteromalus puparum . The full‐length cDNA of PraAry is 2 270 nucleotides and contains a 2 121 nucleotide open reading frame encoding 707 amino acids with calculated molecular weights of approximately 83 kDa. Analysis of the primary protein sequence revealed that it possesses a signal peptide of 16 amino acids at the N‐terminus and contains two highly conserved storage protein signature motifs. According to both phylogenetic analysis and the criteria for amino acid composition, PraAry belongs to the subfamily of arylphorin‐type storage protein (1.42% methionine and 18.82% aromatic amino acids). Reverse transcription – polymerase chain reaction analysis indicated that the transcriptional level of PraAry mRNA in P . rapae pupae fat body is inducible in response to parasitism by P . puparum .